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Binary complex of the papg receptor-binding domain bound to GBO4 receptor

Analyse Binary complex of the papg receptor-binding domain bound to GBO4 receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1J8R
Type: protein
Length: 196 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyelonephritic adhesin
UniProt: Q47450
Ligands: BGC, GAL, GLA, NGA

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyelonephritic adhesin	protein	196	2% helix, 57% strand	Q47450

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · chains A
GAL · beta-D-galactopyranose · sugar · chains A
GLA · alpha-D-galactopyranose · sugar · chains A
NGA · 2-acetamido-2-deoxy-beta-D-galactopyranose · sugar · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 3 modified, 1 disulfide (engineered, disulfide).

Compared structures

1J8R · Binary complex of the papg receptor-binding domain bound to GBO4 receptor · the same entry in another collection · chain A against A, TM-score 1.00
Q47450 · AlphaFold monomer V2.0 prediction for fimbrial adhesin papgii (Q47450) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q47450
Elsewhere: RCSB PDB 1J8R · PDBe 1J8R · UniProt Q47450

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